TNFR2 (Aglyco-Fc-Fusion)
TNFR2 (Aglyco-Fc-Fusion)
TNFR2 is a single-pass type I membrane protein and the member of TNFR superfamily containing 4 cysteine-rich domains (CRD) repeats. In addition to the full length membrane-anchored form, soluble TNFR2 can be generated via two distinct mechanisms: (1) shedding via proteolytic processing of the full membrane anchored from, and (2) translation from an alternatively spliced message encoding the extracellular domains of TNFR2.
Interacting protein(s): TNF (P7113T), TNF (P7113F), TNF (P7113M), LT-a (P7006M)
Related products: TNF-Receptor Superfamily
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Quick Specs
Species: | Human |
Catalog No.: | P7022G |
Synonym: | TNFRSF1B, p75, p80, TNF-alpha receptor, CD120b |
Tag: | Aglycosylated mouse IgG2a-Fc |
GenBank Accession: | NM_001066 |
SwissPro Accession: | P20333 |
Construction: | h.TNFR2 (L23-D257)-m.IgG-Fc |
Expression host: | 293T |
MW (calculated): | 52,207 daltons |
MW (SDS-PAGE): | 60 Kd |
Abs 0.1% (= 1 mg/ml): | 1.114 |
Purity: | 95 % |
Description
TNFR2 is a single-pass type I membrane protein and the member of TNFR superfamily containing 4 cysteine-rich domains (CRD) repeats. In addition to the full length membrane-anchored form, soluble TNFR2 can be generated via two distinct mechanisms: (1) shedding via proteolytic processing of the full membrane anchored from, and (2) translation from an alternatively spliced message encoding the extracellular domains of TNFR2. TNFR2 is the receptor with high affinity for TNF-α and approximately 5-fold lower affinity for homotrimeric lymphotoxin-alpha.
TNFR2 mediates most of the metabolic effects of TNF-α. The soluble form of TNFR2 can block TNF-alpha-induced apoptosis and has been developed as a therapeutic biologics, Enbrel, for treating chronic inflammatory diseases such as rheumatoid arthritis (RA). The extracellular CRD regions of the TNFR2 and TNFR1 are quite similar. In contrast, the intracellular domains of the two TNF receptors are entirely unrelated, indicating different modes of signaling and functions.
At its intracellular side, TNFR2 also binds to the TRAF1/TRAF2 heterocomplex complex which recruits the apoptotic suppressors BIRC2 and BIRC3 and additional 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TRAF2, which mediates anti-apoptotic signals.
Amino Acid Sequence.
References
1. Chen Y, Jiang M, Chen X. Therapeutic potential of TNFR2 agonists: a mechanistic perspective. Front Immunol. 2023;14:1209188. Epub 20230817. doi:
2. A second tumor necrosis factor receptor gene product can shed a naturally occurring tumor necrosis factor inhibitor. Kohno T., Brewer M.T., Baker S.L., Schwartz P.E., King M.W., Hale K.K., Squires C.H., Thompson R.C., Vannice J.L. Proc. Natl. Acad. Sci. U.S.A. 87:8331-8335 (1990)
3. Identification and characterization of a novel spliced variant that encodes human soluble tumor necrosis factor receptor 2. Lainez B., Fernandez-Real J.M., Romero X., Esplugues E., Canete J.D., Ricart W., Engel P. Int. Immunol. 16:169-177 (2004)
4. Two human TNF receptors have similar extracellular, but distinct intracellular, domain sequences. Dembic Z., Loetscher H., Gubler U., Pan Y.C., Lahm H.-W., Gentz R., Brockhaus M., Lesslauer W. Cytokine 2:231-237(1990)
5. Biochemical properties of the 75-kDa tumor necrosis factor receptor. Characterization of ligand binding, internalization, and receptor phosphorylation. Pennica D., Lam V.T., Mize N.K., Weber R.F., Lewis M., Fendly B.M., Lipari M.T., Goeddel D.V. . Biol. Chem. 267:21172-21178(1992)